UniProt Accession

 LSMD1_HUMAN; Q9BRA0; Q8N4M0 

Genbank Protein ID

 AF530060; BC006407; BC033861; BC051846; BC059944 

Genbank Nucleotide ID

 AAQ09944.1; AAH06407.1; AAH33861.1; AAH51846.1; AAH59944.1 

Protein Name

 LSM domain-containing protein 1 

Protein Synonyms/Alias

 Phosphonoformate immuno-associated protein 2 

Gene Name

 LSMD1 

Gene Synonyms/Alias

 MAK31; PFAAP2 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
99	QLEALLNKTMRIRMT	ubiquitination	[1, 2, 3]
134	GSAQEFLKPSDSFSA	ubiquitination	[2]

Reference

 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

Functional Description

 Component of the N-terminal acetyltransferase C (NatC) complex which may catalyze acetylation of N-terminal methionine residues. 

Sequence Annotation

 MOD_RES 22 22 Phosphoserine.
 MOD_RES 25 25 Phosphoserine.
 MOD_RES 29 29 Phosphoserine.  

Keyword

 Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 125 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 

Interpro

 IPR010920; LSM_dom.
 IPR001163; Ribonucl_LSM.
 IPR006649; Ribonucl_LSM_euk/arc. 

Pfam

 PF01423; LSM 

SMART

 SM00651; Sm 

PROSITE

  

PRINTS